Research workbench
Crystal structures of true enzymatic reaction intermediates: aspartate and glutamate ketimines in aspartate aminotransferase
Analyse Crystal structures of true enzymatic reaction intermediates: aspartate and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MAP
- Type
- protein
- Length
- 401 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate aminotransferase
- EC
- 2.6.1.1
- UniProt
- P00508
- Ligands
- KET
- Pockets
- 3 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate aminotransferase (EC 2.6.1.1) | protein | 401 | 47% helix, 14% strand | P00508 |
Ligands and binding sites
- KET · 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethylene)-amino]-succinic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 241 | 0.62 | 0.81 | 36 | KET |
| 2 | 255 | 0.55 | 0.77 | 26 | empty |
| 3 | 120 | 0.44 | 0.77 | 20 | empty |
Compared structures
- 1MAP · Crystal structures of true enzymatic reaction intermediates: aspartate and glutamate… · the same entry in another collection · chain A against A, TM-score 1.00
- P00508 · AlphaFold monomer V2.0 prediction for aspartate aminotransferase, mitochondrial (P00508) · a predicted model of the same protein · chain A against A, TM-score 0.98
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P00508
- Elsewhere: RCSB PDB 1MAP · PDBe 1MAP · UniProt P00508
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